Coherent X-ray diffractive imaging of protein crystals.
The technique of coherent X-ray diffraction imaging (CXDI) has recently shown great promise for the study of inorganic nanocrystals. In this work the CXDI method has been applied to the study of micrometer-size protein crystals. Finely sampled diffraction patterns of single crystals were measured and iterative phase-retrieval algorithms were used to reconstruct the two-dimensional shape of the crystal. The density maps have limited reproducibility because of radiation damage, but show clear evidence for crystal facets. Qualitative analysis of a number of single-crystal diffraction peaks indicates the presence of inward surface contraction on 2 microm size crystals. A survey of several hundred diffraction patterns yielded a number of examples with dramatic single-sided streaks, for which a plausible model is constructed.
Boutet
Sébastien
S
Department of Physics, University of Illinois, Urbana, IL 61801, USA. sboutet@slac.stanford.edu
Robinson
Ian K
IK
D000465:Algorithms; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D007090:Image Interpretation, Computer-Assisted / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D041623:Tomography, Optical Coherence / Q000379:methods*; D014961:X-Ray Diffraction / Q000379:methods*
D011506:Proteins